Issue 10, 2020

The robustness of the terminal emitter site in major LHCII complexes controls xanthophyll function during photoprotection

Abstract

Xanthophylls in light harvesting complexes perform a number of functions ranging from structural support to light-harvesting and photoprotection. In the major light harvesting complex of photosystem II in plants (LHCII), the innermost xanthophyll binding pockets are occupied by lutein molecules. The conservation of these sites within the LHC protein family suggests their importance in LHCII functionality. In the present work, we induced the photoprotective switch in LHCII isolated from the Arabidopsis mutant npq1lut2, where the lutein molecules are exchanged with violaxanthin. Despite the differences in the energetics of the pigments and the impairment of chlorophyll fluorescence quenching in vivo, we show that isolated complexes containing violaxanthin are still able to induce the quenching switch to a similar extent to wild type LHCII monomers. Moreover, the same spectroscopic changes take place, which suggest the involvement of the terminal emitter site (L1) in energy dissipation in both complexes. These results indicate the robust nature of the L1 xanthophyll binding domain in LHCII, where protein structural cues are the major determinant of the function of the bound carotenoid.

Graphical abstract: The robustness of the terminal emitter site in major LHCII complexes controls xanthophyll function during photoprotection

Supplementary files

Article information

Article type
Paper
Submitted
04 май 2020
Accepted
12 авг 2020
First published
14 авг 2020
This article is Open Access
Creative Commons BY-NC license

Photochem. Photobiol. Sci., 2020,19, 1308-1318

The robustness of the terminal emitter site in major LHCII complexes controls xanthophyll function during photoprotection

F. Saccon, M. Durchan, T. Polívka and A. V. Ruban, Photochem. Photobiol. Sci., 2020, 19, 1308 DOI: 10.1039/D0PP00174K

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